Copper ions and hypochlorite are mainly responsible for oxidative inactivation of paraoxon-hydrolyzing activity in human high density lipoprotein

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dc.contributor.authorS D Nguyen-
dc.contributor.authorJ R Kim-
dc.contributor.authorM R Kim-
dc.contributor.authorTae Sook Jeong-
dc.contributor.authorD E Sok-
dc.date.accessioned2017-04-19T09:00:58Z-
dc.date.available2017-04-19T09:00:58Z-
dc.date.issued2004-
dc.identifier.issn0378-4274-
dc.identifier.uri10.1016/j.toxlet.2003.12.011ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6452-
dc.description.abstractParaoxon-hydrolyzing activity of HDL (HDL-PON1) is known to lose its activity under oxidative stress condition. Here, we attempted to elucidate the possible causes for the oxidative inactivation of HDL-PON1 in vivo system. of various oxidative systems, ascorbate/Cu2+ system was the most potent in inactivating the paraoxon-hydrolyzing activity of purified PON1 (PON1). The inclusion of Cu2+ (0.5-2.0μM) remarkably enhanced the ascorbate (0.5mM)-induced inactivation of purified PON1. A similar inactivation was also obtained with HDL-PON1, although to a less extent. The inactivation of PON1, either purified or HDL-bound, by ascorbate/Cu2+ was prevented by catalase or thiols, but not general hydroxyl radical scavengers, suggesting the involvement of Cu2+-catalyzed oxidation in PON1 inactivation. In addition, some lipids such as oleic acid or dioleoylphophatidylglycerol expressed a partial protection. Noteworthy, HDL-PON1, but not purified PON1, was inactivated significantly in a concentration-dependent manner by Cu 2+ alone, and the inactivation of HDL-PON1 by Cu2+ was prevented by catalase, consistent with the intermediacy of H2O 2 in Cu2+-induced inactivation of HDL-PON1. Separately, PON1, either purified or HDL-bound, was found to be susceptible to hypochlorite oxidation. While the susceptibility to hypochlorite below 1mM was similar between purified PON1 and HDL-PON1, the inactivation of HDL-PON1 by hypochlorite at >1mM seemed to be interfered by the membrane. Moreover, the sequential inclusion of hypochlorite and ascorbate/Cu2+ showed a cooperative action in inactivating HDL-PON1. Based on these results, it is proposed that copper ion-catalyzed oxidation and hypochlorite oxidation may be mainly responsible for the loss of HDL-associated paraoxonase1 activity.-
dc.publisherElsevier-
dc.titleCopper ions and hypochlorite are mainly responsible for oxidative inactivation of paraoxon-hydrolyzing activity in human high density lipoprotein-
dc.title.alternativeCopper ions and hypochlorite are mainly responsible for oxidative inactivation of paraoxon-hydrolyzing activity in human high density lipoprotein-
dc.typeArticle-
dc.citation.titleToxicology Letters-
dc.citation.number3-
dc.citation.endPage208-
dc.citation.startPage201-
dc.citation.volume147-
dc.contributor.affiliatedAuthorTae Sook Jeong-
dc.contributor.alternativeNameNguyen-
dc.contributor.alternativeName김주령-
dc.contributor.alternativeName김미리-
dc.contributor.alternativeName정태숙-
dc.contributor.alternativeName석대은-
dc.identifier.bibliographicCitationToxicology Letters, vol. 147, no. 3, pp. 201-208-
dc.identifier.doi10.1016/j.toxlet.2003.12.011-
dc.subject.keywordCu2+-
dc.subject.keywordHDL-
dc.subject.keywordHOCl-
dc.subject.keywordHydroxyl radicals-
dc.subject.keywordOxidative inactivation-
dc.subject.keywordPON1-
dc.subject.localCu2+-
dc.subject.localHDL-
dc.subject.localHOCl-
dc.subject.localhydroxyl radical-
dc.subject.localHydroxyl radicals-
dc.subject.localHydroxyl radical-
dc.subject.localOxidative inactivation-
dc.subject.localPON1-
dc.description.journalClassY-
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Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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